NADH dehydrogenase in Neurospora crassa contains myristic acid covalently linked to the ND5 subunit peptide

• Tipo: Artigo em Revista Científica Internacional
• Data: 2000

Autores

plesofsky, n (Autor) Outra; gardner, n (Autor) Outra; videira, a (Autor) ICBAS; brambl, r (Autor) Outra

Revista

Título: Biochimica et Biophysica Acta - Molecular Cell Research

Vol. 1495

Páginas: 223-230

ISSN: 0167-4889

Editora: Elsevier

Indexação

ISI Web of Knowledge - 10 Citações

Scopus - 11 Citações

Outras Informações

ID Authenticus: P-001-0SM

DOI: 10.1016/S0167-4889(99)00170-6

Abstract (EN): The mitochondrial, proton-pumping NADH:ubiquinone oxidoreductase consists of at least 35 subunits whose synthesis is divided between the cytosol and mitochondria; this complex I catalyzes the first steps of mitochondrial electron transfer and proton translocation. Radiolabel from [H-3]myristic acid was incorporated by Neurospora crassa into the mitochondrial-encoded, similar to 70 kDa ND5 subunit of NADH dehydrogenase, as shown by immunoprecipitation. This myristate apparently was linked to the peptide through an amide linkage at an invariant lysine residue (Lys546), based upon analyses of proteolysis products, The myristoylated lysine residue occurs in the predicted transmembrane helix 17 (residues 539-563) of ND5. A consensus amino acid sequence around this conserved residue exists in homologous subunits of NADH dehydrogenase. Cytochrome c oxidase subunit 1, in all prokaryotes and eukaryotes, contains this same consensus sequence surrounding the lysine which is myristoylated in N. crassa. (C) 2000 Elsevier Science B.V. All rights reserved.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 8